G. Frahry et P. Schopfer, INHIBITION OF O-2-REDUCING ACTIVITY OF HORSERADISH-PEROXIDASE BY DIPHENYLENEIODONIUM, Phytochemistry, 48(2), 1998, pp. 223-227
Plant cells respond to pathogen attack with a burst of H2O2 secretion.
The question whether this defense reaction is catalysed by a NAD(P)H
oxidase similar to the NADPH oxidase of phagocytic leukocytes in mamma
ls or by an extracellular peroxidase is presently a matter of controve
rsial debate. The observation that H2O2 production by plant cells can
be inhibited by diphenyleneiodonium (DPI), a potent inhibitor of the m
ammalian NADPH oxidase, has fostered the view that a mammalian-type en
zyme is responsible for the H2O2 production by plant cells. Here we sh
ow that DPI inhibits the NADH-dependent H2O2 production by horseradish
peroxidase in the same concentration range as previously used for the
inhibition of putative NADPH oxidase activity in plants. The peroxida
tive activity normally used for assaying peroxidase is not affected by
DPI, indicating that the inhibitor specifically interferes with a par
tial reaction that is exclusively involved in the O-2 reducing activit
y of the enzyme. (C) 1998 Elsevier Science Ltd. All rights reserved.